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Database: UniProt
Entry: A0A0F4ZL59_9PEZI
LinkDB: A0A0F4ZL59_9PEZI
Original site: A0A0F4ZL59_9PEZI 
ID   A0A0F4ZL59_9PEZI        Unreviewed;      2546 AA.
AC   A0A0F4ZL59;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKA30866.1};
GN   ORFNames=TD95_000725 {ECO:0000313|EMBL:KKA30866.1};
OS   Thielaviopsis punctulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX   NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA30866.1, ECO:0000313|Proteomes:UP000033483};
RN   [1] {ECO:0000313|EMBL:KKA30866.1, ECO:0000313|Proteomes:UP000033483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA30866.1};
RA   Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKA30866.1}.
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DR   EMBL; LAEV01000214; KKA30866.1; -; Genomic_DNA.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000033483; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..427
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2462..2539
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2546 AA;  276495 MW;  57EA58CE039F8727 CRC64;
     MPCGESPVPP VAVVGFGMRL PGKISTSEDL WSLIVNKRDA RAPIPASRWD AKTWKNNHAT
     DHGYFLDEET DLKKFDSSMF SMSRTELESL DPRQRILLEV VWECMENAGQ KEWRGTRTGV
     FVGSFSQDWM EMTARDPLMK GVFRIYNGAD FYLPNRISYE YNLSGPSVAV QAACASGLTA
     VHEACTALYN GECKGAIAAG TSILLSPLVV EVMTQQGVLS PNGSCSTFSA EADGYARAES
     VNAVYLKLLD DALRDGDPIR GVIRGTALSA NGKTNGMLLP DAKYQQKTIE EAYKAAGITD
     LTQTPFVECH GTGTPVGDPI EVRGVINAFG TEGEHGKPTY IGSHKPNLGH SEGASGINSL
     IKAVLAVENG IIPPNIKFNK PNPQIPFDTA RLIVPVEPTP FPACRATRVS INSFGIGGAN
     AHLVLDSAAE FLHTYPGVPP PFPAPPPGSH TIWPRMVVVT SSNMASLNQR VHDIKQYLDL
     RPRTVLNDVA YTLANRRSHL TYRSFAVVTH SQNEPFEFEK PQISYAKPPA PVFVFTGQGA
     QWGGMASDLL RISPVFAESI RTMDAALAKL GPAAPSWTLE KMIAAKDDET KALFDKPEFS
     QPLCTAVQVG VLQFMQACGV QHTAVVGHSS GEIAAAYAAG GLTLQEAIVV SYLRGWAVKV
     EQAKGTGTKG GMAAVGLGKT EAEKYVCPGV VVACENSPQS VTLSGDEDVL DAALSEISKS
     SVFTRRLKVD VAYHSHHMKN VGEVYDTALS PQLAKSKKKL SVPFYSSVTL EKVGNSEIFD
     TAYWCKNLKS PVRFNDAVQS IISDNPDKDL VFLEIGPHST LQGPLRQIFQ VAAQNGRFLG
     KNFLYIPTLL RNVPAKISLT KAAGHAFSFG IPVNFGILTP PPTPTSKPLT DLPRYPWDRN
     VEFWNESRLS VAHRFPKYPR HELLGTRGLE GTDLEPTWRN IIAPNDIPWV QDHVVGSDVI
     LPCAGYVSMV GEALRQLSGD DNAGYTLREV EVKSALILPD NRAVEVMTTA RLVRPSTFGE
     PGSWYEFSIS SYNGSSWMQL YSAKGRSGAE SGYPAKMPLQ PTHKFSRKVS SEVWYDAFAH
     VGLAYGPKFQ GLASLSAVPG EPLGSSTIKT FDEDISKKSS ATYTQHPTTL DCALQLGLFA
     STSGLPKRLS AVLPTAIDFV YVKPASNLKS LYTQATFQKN QNKGKVLGGH SCRALDPQTF
     ETIIDIQNCR HTHFQIKSKS NSIGNGFDHV GAASLVWRPD INFCKPEVTM KPLPDVYRPS
     KVLLEKIVAL CVLHSVDVMT IEKAKVGSND ISFVEPHLKK YIAWLSTAKA EMLSGTGSWS
     RLCPEAQHFA SMSLEQRENE FSLVEQQVAA MSSHNSDMGV MMRICRKLAE NMYLLATGKA
     NSVEIMFSRT SESLASWYDF LGNLLDFSEY FKLSGHANPN LRVLEIGAGT GASSARVLQA
     LVADSNKPRY GEYTFTDVSS GFFEAARDRL KEYPNIKYKV LDISRDPAEQ GFELGSYDLI
     VASNVIHATP NLNQTLTNTR ALLRDGGRFY LQEVVGPTNV FGFLAGVFSG WWMGEFDGRP
     NAPTVSVDRW HQELIAAGFS GAGDAVLDDD ETLTYLANIV TRAMPVKNQA PEFKTATIIY
     EKEKPTFASS LSSSLAANGF GVSWEKLEDF ASSSVTPSVV ISALDLEHPF FVGLTSRKYA
     LLTNIILNLS TPLIWLTCPA QVDVENPHYA QIIGLGRNVR NELSKKFVTI ELGSSDTASA
     KAVTKIVEDL AVNLTNVSSS SHYDADSEYF VKDGIVYTSR YETLMLDDEL AEQSHERTSV
     TLISSEVGSF NKPKWIEESV VLALAANDVE VDVQATSLNY KYHDVMLYSN SLEGSENHIG
     VEAAGVVSRV GALVDNIKVG DRVVLIAAGA VSSVKVVNKD LVVKIPDSLD FEQAATLPIS
     YLTAIHALSN LKSGQTVLIH SGSGSLGQAA IQVAQMLGAT VFTTAGTEEK ADFITSQFGI
     PPSRIFSSCD ISFAYGVMFS TLGKGVDVVF NTLSGELLQA SWGCVSPNGK MINMTRDSEQ
     LPASAQNSSR TLISLNMGLM ISERPSEVNL LLNKTLDHFS RGHIKPITIS EVFSAKDVSH
     GFSHIQANKH MGRVVLTFNV SESLAAFSSR KKQSIAFSSF KTYLLAGGMG GLGKSIATWM
     VEHGARKFIF LSRSAGISEA DKAFITELES QGCYVNAIAS SVADASAVEK AVQSAPSRLG
     GIMQLSMVLS DASLSDMTYE QWMIPQGPKV DGTWNLHNAT VDTPLDFFVL FSSISSVAGN
     PGQANYSSAG TFIEAFAQYR QRQGLACSVV NIGAVQGVGY ISRHKTVSST ITSMGQSMLQ
     EQDVLDSVQV SIQRPFNGCE FSEPVGNDKN GSFLFSGQLV TGLRSTRVTS NADCHVPWKR
     DIRTSIVQVD EAIMIEQASA FDSDTSGTAA SNSANDIDAP NTILRDLVRE VSSDTQKLTA
     KATMDTLVHN IGRVLCRILL QPEDCLENGV TLMQMGLDSM VGIEVRNWWK RTFPGDISVL
     QIINAVTIER LAQMALEALQ KNAQAI
//
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